Hypothetical view of the dystrophin‐associated complex of proteins and glycoproteins at the surface of the muscle fibre. Dystrophin,
the protein that is lacking in Duchenne muscular dystrophy and is defective in the milder Becker muscular dystrophy, appears
to be the key protein required for effective assembly of this complex, elucidation of which has proved an interesting example
of the interaction between positional cloning and biochemical investigation. Mutations in the genes for the various sarcoglycans
have been found to underlie some of the limb‐girdle muscular dystrophies (LGMD): α‐Sarcoglycan – LGMD 2D, β‐Sarcoglycan – LGMD 2E, γ‐Sarcoglycan – LGMD 2C, δ‐Sarcoglycan – LGMD 2F. A large proportion of congenital muscular dystrophy cases have proved to involve mutations in the α‐chain of merosin,
the link of this complex into the basement membrane. The muscle‐specific isoform of neural nitric oxide synthase, μNOS, and
the dystrophin‐like protein, dystroglycan, are also linked into this complex and disruption of this complex may compromise
their functions and perhaps contribute to some aspects of the pathology of the dystrophinopathies. Other dystrophies are ascribed
to proteins that do not appear to be part of this complex, some associated with the cell surface, some with the nuclear membranes
and some with the sarcoplasm (for review, see Cohn and Campbell (2000) Molecular basis of muscular dystrophies. Muscle and Nerve 23: 1456–1471).

Trial on use of morpholino antisense oligonucleotides to induce skipping of exons such as to restore open reading frame in the mutated dystrophin gene http://www.clinicaltrials.gov/ct/show/NCT00159250?order=1